CN116120431A - Antioxidant collagen polypeptide, preparation method and application thereof - Google Patents
Antioxidant collagen polypeptide, preparation method and application thereof Download PDFInfo
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- CN116120431A CN116120431A CN202211669217.2A CN202211669217A CN116120431A CN 116120431 A CN116120431 A CN 116120431A CN 202211669217 A CN202211669217 A CN 202211669217A CN 116120431 A CN116120431 A CN 116120431A
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- 102000008186 Collagen Human genes 0.000 title claims abstract description 57
- 108010035532 Collagen Proteins 0.000 title claims abstract description 57
- 229920001436 collagen Polymers 0.000 title claims abstract description 57
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 54
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 44
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 43
- 230000003078 antioxidant effect Effects 0.000 title claims abstract description 32
- 239000003963 antioxidant agent Substances 0.000 title claims abstract description 22
- 238000002360 preparation method Methods 0.000 title claims abstract description 13
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 4
- 108090000790 Enzymes Proteins 0.000 claims description 10
- 102000004190 Enzymes Human genes 0.000 claims description 10
- 229940088598 enzyme Drugs 0.000 claims description 10
- 241000283690 Bos taurus Species 0.000 claims description 9
- 239000004365 Protease Substances 0.000 claims description 8
- 238000000034 method Methods 0.000 claims description 8
- 229940055729 papain Drugs 0.000 claims description 8
- 108090000526 Papain Proteins 0.000 claims description 6
- 239000002537 cosmetic Substances 0.000 claims description 6
- 239000000413 hydrolysate Substances 0.000 claims description 6
- 235000019834 papain Nutrition 0.000 claims description 6
- 108091005658 Basic proteases Proteins 0.000 claims description 4
- 235000013305 food Nutrition 0.000 claims description 4
- 238000004007 reversed phase HPLC Methods 0.000 claims description 4
- 239000000758 substrate Substances 0.000 claims description 4
- 238000004255 ion exchange chromatography Methods 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 238000010532 solid phase synthesis reaction Methods 0.000 claims description 2
- 101150116862 KEAP1 gene Proteins 0.000 abstract description 11
- 230000003993 interaction Effects 0.000 abstract description 4
- 230000004792 oxidative damage Effects 0.000 abstract description 4
- 102000004169 proteins and genes Human genes 0.000 abstract description 4
- 108090000623 proteins and genes Proteins 0.000 abstract description 4
- 150000003254 radicals Chemical class 0.000 description 6
- 230000000694 effects Effects 0.000 description 5
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- 210000000988 bone and bone Anatomy 0.000 description 4
- HHEAADYXPMHMCT-UHFFFAOYSA-N dpph Chemical compound [O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1[N]N(C=1C=CC=CC=1)C1=CC=CC=C1 HHEAADYXPMHMCT-UHFFFAOYSA-N 0.000 description 4
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- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 3
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- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
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- 229910021641 deionized water Inorganic materials 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
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- 238000000502 dialysis Methods 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 230000000378 dietary effect Effects 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 230000004064 dysfunction Effects 0.000 description 1
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- 238000003379 elimination reaction Methods 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000007760 free radical scavenging Effects 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 239000010985 leather Substances 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 239000002366 mineral element Substances 0.000 description 1
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- 230000001953 sensory effect Effects 0.000 description 1
- 238000004088 simulation Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
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- 239000006228 supernatant Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/65—Collagen; Gelatin; Keratin; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Abstract
The invention provides an antioxidant collagen polypeptide, a preparation method and application thereof, wherein the amino acid sequence of the collagen polypeptide is IDGRPGPIGPA or ISGPHypGPHYpGPA. The collagen polypeptide provided by the invention has antioxidant activity, can be combined with Keap1 to inhibit the interaction of Nrf2-Keap1 protein, and can effectively protect oxidative damage cells.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to a collagen polypeptide, a preparation method and application thereof.
Background
Oxidative stress is a pathological state caused by unbalance of production and elimination of intracellular free radicals, and causes dysfunction of cells, tissues and organs, and is considered to be one of important induction factors causing occurrence of various diseases. Some external factors, such as environmental pollution, irregular diet and lifestyle, etc., can cause excessive accumulation of free radicals in the body, thereby causing oxidative stress. More and more studies have shown that oxidative stress increases gradually with age, further leading to the onset and progression of age-related diseases.
Collagen peptide is a small molecular active substance obtained by hydrolyzing collagen under proper conditions, and has good biological activity, such as anticancer, blood pressure lowering, antiinflammatory, mineral element absorption promoting, etc. In addition, collagen peptides have been found to have good antioxidant activity, capable of exerting antioxidant effects by good scavenging action on different types of free radicals or by promoting activation of antioxidant enzyme activity in the body and elevation of non-enzymatic antioxidant levels. Studies have shown that the intake of dietary antioxidants helps to prevent and alleviate oxidative stress in the body, thereby reducing to some extent the incidence of oxidative stress-like diseases.
In Chinese patent No. 111334551B, a production process of collagen peptide of cow leather is disclosed, which comprises S1 cleaning, S2 denaturation, S3 enzymolysis, S4 centrifugation, S5 enzyme deactivation, S6 impurity removal and S7 finished product. The invention has the following advantages and effects: the application adopts the combined action of the ultrasonic process, the denaturation process and the enzymolysis process, and can be conveniently suitable for cowhide in various producing areas; the collagen peptide product produced by the process has good solubility and dispersibility, good sensory quality and high yield, and a large amount of active polypeptide in the product has stronger antioxidant capacity. However, the product has a large amount of components with weak antioxidant capacity, weak DPPH free radical scavenging capacity and limited total antioxidant activity, and the half-inhibition concentration is above 30 mg/mL.
In addition, in Chinese patent CN108250291B, an antioxidant collagen polypeptide is disclosed, which is characterized in that: the amino acid sequence of the antioxidant collagen polypeptide is SSGPPVPGPMGPMGPR, and the antioxidant collagen polypeptide peptide chain contains two methionine residues. However, this patent discloses only that the polypeptide has antioxidant activity, and does not disclose that it is capable of binding to Keap1 to inhibit the interaction of Nrf2-Keap1 protein.
Accordingly, it is an object of the present invention to provide a small-molecule collagen polypeptide capable of inhibiting the interaction of Nrf2-Keap1 protein by binding to Keap1, thereby exerting antioxidant activity.
Disclosure of Invention
The invention aims to provide a small molecular peptide which can be combined with Keap1 to inhibit the interaction of Nrf2-Keap1 protein so as to play an antioxidant activity, a preparation process and application thereof. In order to achieve the purpose of the invention, the following technical scheme is adopted:
in one aspect, the invention relates to a collagen polypeptide, wherein the amino acid sequence of the collagen polypeptide is IDGRPGPIGPA or ISGPHypGPHYpGPA, wherein Hyp is the abbreviation of hydroxyproline.
The invention also relates to a food, which contains the collagen polypeptide. The amount of the collagen polypeptide used in the food is not particularly limited, and may be, for example, 0.5wt% to 5 wt%.
In another aspect, the invention also relates to a cosmetic comprising the collagen polypeptide. The amount of the collagen polypeptide used in the cosmetic is not particularly limited, and may be, for example, 0.1wt% to 5.0 wt%.
The invention also relates to a preparation method of the collagen polypeptide, the collagen polypeptide carries out enzymolysis catalysis on bovine bone collagen by alkaline-papain, and the enzymolysis conditions are as follows: the pH is 7-8, the temperature is 55-65 ℃, the enzymolysis time is 80-160 min, the substrate concentration is 20-30% (w/v), the total enzyme dosage is 6000-10000U/g, and the enzyme adding ratio of alkaline protease to papain is 1:2-4; separating the collagen hydrolysate by ion chromatography and reversed phase high performance liquid chromatography.
Preferably, the collagen polypeptide is catalyzed by alkaline papain to perform enzymolysis on bovine collagen, and the enzymolysis conditions are as follows: the pH is 7.7, the temperature is 59.6 ℃, the enzymolysis time is 120 min, the substrate concentration is 25% (w/v), the total enzyme dosage is 8396U/g, and the enzyme adding ratio of alkaline protease to papain is 1:3. Separating the collagen hydrolysate by ion chromatography and reversed phase high performance liquid chromatography.
Although the collagen polypeptide of the present invention can be prepared by sea cucumber, the collagen polypeptide of the present invention can also be prepared by solid phase synthesis.
In another aspect, the invention also relates to the use of the collagen polypeptide described above for the preparation of an antioxidant, or for the preparation of a cosmetic having an antioxidant effect.
The beneficial technical effects of the invention are as follows:
the invention discloses an antioxidant collagen polypeptide (IDGRPGPIGPA affinity= -9.1 kcal/mol, ISGPHypGPHYpGPA affinity= -9.2 kcal/mol) capable of inhibiting Nrf2-Keap1 protein interaction by combining with Keap1 and a preparation method thereof, wherein bovine collagen is subjected to enzymolysis catalysis by alkaline-papain, combination separation, identification, molecular docking simulation and chemical synthesis to obtain the antioxidant collagen polypeptide capable of inhibiting Nrf2-Keap1 protein interaction by combining with Keap1, so that the antioxidant collagen polypeptide can effectively protect cells from oxidative damage. The collagen polypeptide adopts bovine collagen as a raw material and has the advantages of wide sources and higher protein content.
Drawings
Fig. 1: the ability of antioxidant collagen polypeptides to scavenge DPPH and ABTS free radicals;
fig. 2: antioxidant collagen polypeptide pair H 2 O 2 Inducing the protective effect of oxidative damage cells.
Detailed Description
The present invention will be further described in detail below with reference to specific embodiments and with reference to the accompanying drawings, in order to make the objects, technical solutions and advantages of the present invention more apparent.
Example 1: preparation of collagen polypeptide
The preparation method provided by the invention comprises the following steps:
(1) Extraction of collagen hydrolysate of ox bone
Mixing defatted and decalcified bovine bone with deionized water to make the substrate concentration 25% (w/v), pH of the system 7.7, reaction temperature 59.6deg.C, enzymolysis time 120 min, total enzyme dosage 8396U/g, and enzyme adding ratio of alkaline protease and papain 1:3. After the enzymolysis reaction is finished, collecting supernatant by centrifugation, and obtaining the collagen hydrolysate of the bovine bone after filtration and freeze drying.
(2) Separation, purification and identification of enzymatic products
The crude bovine collagen hydrolysate was subjected to preliminary separation by DEAE52 cellulose anion chromatography using a buffer containing NaCl at different concentrations (0, 0.1, 0.2, 0.3, 0.4 and 1.0M) at a flow rate of 1 mL/mm, and the separation was collected under the same peak under 280 nm monitoring, and subjected to dialysis desalting treatment. Separating the optimal antioxidant active components by reverse phase high performance liquid chromatography, and selecting C18 chromatographic column (10 mm ×250 mm) with detection wavelength of 280 nm, sample injection amount of 50 μl, column temperature of 30deg.C, flow rate of 1.0 mL/min, mobile phase A of ultrafiltration water containing 0.05% TFA, and mobile phase B of acetonitrile containing 0.05% TFA. The polypeptide elution procedure was: the first 35 min,5-55% mobile phase B;35-40 min,55-95% mobile phase B. The antioxidant activity of the different elution components is collected and measured, and the optimal antioxidant active component is taken and the peptide sequence is measured by utilizing LC-MS/MS.
(3) Molecular docking screening and activity verification of antioxidant active peptide
Docking was based on the crystal structure of Keap1 (PDB ID:4 IQK), and the binding capacity of the polypeptide to Keap1 was predicted by using Autodock Vina, and active collagen polypeptides having a high affinity to Keap1 were selected, and the peptide sequence was IDGRPGPIGPA or ISGPHypGPHYpGPA (IDGRPGPIGPA affinity= -9.1 kcal/mol, ISGPHypGPHYpGPA affinity= -9.2 kcal/mol). The affinity of the ligand IQK in Keap1 is-11.3 kcal/mol, and the affinity of the active peptide obtained by screening with the method with Keap1 is higher. The antioxidant activity of the collagen peptide was then synthesized and verified by in vitro chemistry.
As can be seen from FIG. 1, the clearance of DPPH and ABTS free radicals at 5. 5 mM by IDGRPGPIGPA (P1) is 66.58 + -2.87% and 73.78 + -2.04%, respectively, and that of ISGPHypGPHypGPA (P2) at 5 mMThe clearance of DPPH and ABTS free radicals is 59.50 + -1.88% and 64.33 + -3.45%, respectively. As can be seen from FIG. 2, IDGRPGPIGPA (P1) or ISGPHypGPHYpGPA (P2) can effectively increase the cell pair H at a concentration of 50. Mu.M 2 O 2 The resistance to oxidative damage is induced, and the cell activity is obviously improved.
The foregoing description of the embodiments has been provided for the purpose of illustrating the general principles of the invention, and is not meant to limit the invention thereto, but to limit the invention thereto, and any modifications, equivalents, improvements and equivalents thereof may be made without departing from the spirit and principles of the invention.
Claims (8)
1. A collagen polypeptide having the amino acid sequence IDGRPGPIGPA or isgphypgphypppa.
2. A food product comprising one or both of the collagen polypeptides of claim 1.
3. Food product according to claim 2, wherein the total amount of said collagen polypeptide is between 0.5% and 5% by weight.
4. A cosmetic comprising one or two of the collagen polypeptides according to claim 1.
5. The cosmetic according to claim 4, wherein the total amount of said collagen polypeptide is between 0.1 wt.% and 5.0 wt.%.
6. The method for preparing the collagen polypeptide according to claim 1, wherein the collagen polypeptide is prepared by catalyzing enzymolysis of bovine collagen by alkaline papain under the following conditions: the pH is 7-8, the temperature is 55-65 ℃, the enzymolysis time is 80-160 min, the substrate concentration is 20-30% (w/v), the total enzyme dosage is 6000-10000U/g, and the enzyme adding ratio of alkaline protease to papain is 1:2-4; separating the collagen hydrolysate by ion chromatography and reversed phase high performance liquid chromatography.
7. The method for producing a collagen polypeptide according to claim 1, wherein the collagen polypeptide is produced by a solid-phase synthesis method.
8. Use of a collagen polypeptide for the preparation of an antioxidant for improving the antioxidant damage of cells or for the preparation of a cosmetic having antioxidant effect.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202211669217.2A CN116120431A (en) | 2022-12-24 | 2022-12-24 | Antioxidant collagen polypeptide, preparation method and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202211669217.2A CN116120431A (en) | 2022-12-24 | 2022-12-24 | Antioxidant collagen polypeptide, preparation method and application thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN116120431A true CN116120431A (en) | 2023-05-16 |
Family
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202211669217.2A Pending CN116120431A (en) | 2022-12-24 | 2022-12-24 | Antioxidant collagen polypeptide, preparation method and application thereof |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN117903291A (en) * | 2024-03-19 | 2024-04-19 | 如凤凰再生科技发展(成都)有限公司 | Triple helix collagen and preparation method and application thereof |
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2022
- 2022-12-24 CN CN202211669217.2A patent/CN116120431A/en active Pending
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN117903291A (en) * | 2024-03-19 | 2024-04-19 | 如凤凰再生科技发展(成都)有限公司 | Triple helix collagen and preparation method and application thereof |
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